Difference between revisions of "Part:BBa K143034"
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__NOTOC__
 
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<partinfo>BBa_K143034 short</partinfo>
 
<partinfo>BBa_K143034 short</partinfo>
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EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, triggering self-assembly when the EAK16-II peptides are exposed to physiological media or salt solution. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II peptides and these nanofibres can futher aggregate to form a membranous 3D scaffold.  
 
EAK16-II is a sixteen amino acid peptide that self-assembles to form &#946;-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides <cite>1</cite>, triggering self-assembly when the EAK16-II peptides are exposed to physiological media or salt solution. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II peptides and these nanofibres can futher aggregate to form a membranous 3D scaffold.  
  
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LipA is a signal peptide from the B.subtilis genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway<cite>2</cite>. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by ''B. subtilis''.
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LipA is a signal peptide from the ''B. subtilis'' genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway<cite>2</cite>. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by ''B. subtilis''.
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#1 pmid=16061392
 
#1 pmid=16061392
 
#2 pmid=16997527
 
#2 pmid=16997527
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#3 pmid=10974125
 
 
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</biblio>

Latest revision as of 13:47, 18 September 2008

LipA-EAK16-II Fusion Protein


EAK16-II is a sixteen amino acid peptide that self-assembles to form β-sheet structures in an aqueous medium. The alternating positive and negative charges (--++--++) are responsible for creating an electrostatic attraction between adjacent peptides 1, triggering self-assembly when the EAK16-II peptides are exposed to physiological media or salt solution. When examined under SEM, a well-ordered nanofibre structure is formed by the association of the EAK16-II peptides and these nanofibres can futher aggregate to form a membranous 3D scaffold.


LipA is a signal peptide from the B. subtilis genome. In general, signal peptides are responsible for directing preproteins (secretory proteins with a signal peptide region attached)through an appropriate secretory pathway2. LipA has been successfully used in the secretion of heterologous proteins such as cutinase by B. subtilis.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Reference

<biblio>

  1. 1 pmid=16061392
  2. 2 pmid=16997527

</biblio>